I n vitvo studies on the interaction of the pyridoindole antioxidant stobadine with rat liver microsomal P450

References

• Bast A. Is formation of reactive oxygen by cytochrome P-450 perilous and predictable?. Trends in Pharmaceutical Sciences 1986; 7: 266–270
   Web of Science ®Google Scholar
• Bast A., Goossens P. A. L., Savenije-Chapel E. M. Dependence of hydrogen peroxide formation in rat liver microsomes on the molecular structure of cytochrome P-450 substrates: a study with barbiturates and beta-adrenoreceptor antagonists. European Journal of Drug Metabolism and Pharmacokinetics 1989; 14: 93–100
   PubMed Web of Science ®Google Scholar
• Bast A., Savenje-Chapel E. M., Kroeks B. H. Inhibition of mono-oxygenase and oxidase activity of rat hepatic cytochrome P450 by H2-receptor blockers. Xenobiotica 1984; 14: 399–408
   PubMed Web of Science ®Google Scholar
• Benes L., Stolc S. Stobadine. Drugs of the Future 1989; 14: 135–137
   Google Scholar
• Buege J. A., Aust S. D. Microsomal lipid peroxidation. Methods in Enzymology, S. Fleischen, L. Packer. Academic, New York 1978; Vol. 52: 302–310, Part C
   Google Scholar
• Cho A. K., Maynard M. S., Matsumoto R. M., Lindeke B., Paulsen U., Miwa G. T. The opposing effects of N-hydroxyamphetamine and N-hydroxyamphetamine on the H2O2 generated by hepatic cytochrome P-450. Molecular Pharmacology 1982; 22: 465–470
   PubMed Web of Science ®Google Scholar
• Ekstrom G., Ingelman-Sundberg M. Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent on ethanol-inducible cytochrome P-450. Biochemical Pharmacology 1989; 38: 1313–1319, P-450HE1
   PubMed Web of Science ®Google Scholar
• Estabrgok R. W., Wfrringloer J. The measurement of difference spectra: applications to the cytochromes of microsomes. Methods in Enzymology, S. Fleischen, L. Packer. Academic, New York 1978; Vol. 52: 212–220, Part C
   Google Scholar
• Geiger P. J., Bessman S. P. Protein determination by Lowry's method in the presence of sulfydryl reagents. Analytical Biochemistry 1972; 49: 467–473
   PubMed Web of Science ®Google Scholar
• Green M. J., Hill H. A. O. Chemistry of dioxygen. Methods in Enzymology, L. Packer. Academic, New York 1984; Vol. 105: 3–22
   Google Scholar
• Hildebrandt A. G., Roots I. Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes. Archives of Biochemistry and Biophysics 1975; 171: 385–397
   PubMed Web of Science ®Google Scholar
• Horakova L., Briviba K., Sies H. Antioxidant activity of the pyridoindole stobadine in liposomal and microsomal lipid peroxidation. Chemico-Biological Interactions 1992; 83: 85–93
   PubMed Web of Science ®Google Scholar
• Humplova J., Stefek M., Krizanova L., Benes L. Interaction of stobadine with superoxide in vitro. Czechoslovak Physiology 1992; 41: 80, Suppl. 1
   Google Scholar
• Imai I., Ito A., Sato R. Evidence for biochemically different types of vesicles in the hepatic microsomal fraction. Journal of Biochemistry 1966; 60: 417–428
   PubMed Web of Science ®Google Scholar
• Kuthan H., Ullrich V. Oxidase and oxygenase function of the microsomal cytochrome P-450 monooxygenase system. European Journal of Biochemistry 1982; 126: 583–588
   PubMedGoogle Scholar
• O'Brien P. J. Hydroperoxides and superoxides in microsomal oxidations. Hepatic Cytochrome P-450 Monooxygenase System, J. B. Schenkman, D. Kupfer. Pergamon, Oxford 1982; 567–586
   Google Scholar
• Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. Journal of Biological Chemistry 1964; 239: 2370–2378
   PubMed Web of Science ®Google Scholar
• Rossing D., Kahl R., Hildebrandt A. G. Effect of synthetic antioxidants on hydrogen peroxide formation, oxyferro cytochrome P-450 concentration and oxygen consumption in liver microsomes. Toxicology 1985; 34: 67–77
   PubMed Web of Science ®Google Scholar
• Schenkman J. B., Sligar S. G., Cinti D. L. Substrate interaction with cytochrome. Hepatic Cytochrome, J. B. Schenkman, D. Kupfer. Pergamon, Oxford 1982; 587–615; 450, 450, Monooxygenase System
   Google Scholar
• Segel I. H. Biochemical Calculations. Wiley, New York 1976; 208–323
   Google Scholar
• Steenken S., Sundquist A. R., Jovanovic V., Crockett R., Sies H. Antioxidant activity of the pyridoindole stobadine. Pulse radiolytic characterization of one-electron-oxidized stobadine and quenching of singlet molecular oxygen. Chemical Research in Toxicology 1992; 5: 355–360
   PubMed Web of Science ®Google Scholar
• Stefek M., Benes L. Hydrogen peroxide-dependent liver microsomal N-demethylation and N-oxygenation of stobadine, a gamma-carboline antiarrhythmic and cardio-protective agent. Xenobiotica 1989; 19: 627–634
   PubMed Web of Science ®Google Scholar
• Stefek M., Benes L. Pyridoindole stobadine is a potent scavenger of hydroxyl radicals. FEBS Letter 1991; 294: 264–266
   PubMed Web of Science ®Google Scholar
• Stefek M., Benes L., Jergelova M., Scasnar V., Turi-Nagy L., Kocis P. Biotransformation of stobadine, a gamma-carboline antiarrhythmic and cardioprotective agent, in rat liver microsomes. Xenobiotica 1987; 17: 1067–1073
   PubMed Web of Science ®Google Scholar
• Stefek M., Benes L., Kocis P. Biotransformation of stobadine in vivo. Czechoslovak Physiology 1986; 35: 367
   Google Scholar
• Stefek M., Benes L., Zelnik V. N-oxygenation of stobadine, a gamma-carboline antiarrhythmic and cardioprotective agent: the role of flavin-containing monooxygenase. Xenobiotic 1989; 19: 143–150
   PubMed Web of Science ®Google Scholar
• Stefek M., Masarykova M., Benes L. Inhibition of cumene hydroperoxide-induced lipid peroxidation by a novel pyridoindole antioxidant in rat liver microsomes. Pharmacology and Toxicology 1992; 70: 407–411
   PubMedGoogle Scholar
• Stolc S., Bauer V., Benes L., Tichy M. Stobadine, das Heilmittel besonders mit antiarrythmisher und subsidiarer Wirkung bei der Hypoxie des Myokard, sowie ein Verfaren zu ihrer Herstellung. Swiss Patent 1985, 651754
   Google Scholar
• Terelius Y., Ingelman-Sundberg M. Cytochrome P-450-dependent oxidase activity and hydroxyl radical production in micellar and membranous types of reconstituted systems. Biochemical Pharmacology 1988; 37: 1383–1389
   PubMed Web of Science ®Google Scholar
• Werringloer J. Assay of formaldehyde generated during microsomal oxidation reactions. Methods in Enzymology, S. Fleischen, L. Packer. Academic, New York 1978; Vol. 52: 297–302, Part C
   Google Scholar
• Winston G. W., Cederbaum A. I. NADPH-dependent production of oxyradicals by purified components of the rat liver mixed-function oxidase system: oxidation of OH scavenging agents. Journal of Biological Chemistry 1983; 258: 1508–1513
   PubMed Web of Science ®Google Scholar